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O28440

- ASPD_ARCFU

UniProt

O28440 - ASPD_ARCFU

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Protein

Probable L-aspartate dehydrogenase

Gene
nadX, AF_1838
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity.UniRule annotation

Catalytic activityi

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111NAD; via amide nitrogen By similarity
Binding sitei162 – 1621NAD By similarity
Active sitei189 – 1891 By similarity

GO - Molecular functioni

  1. aspartate dehydrogenase activity Source: UniProtKB-EC
  2. NAD binding Source: UniProtKB-HAMAP
  3. NADP binding Source: UniProtKB-HAMAP
  4. oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Source: UniProtKB-HAMAP

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-HAMAP
  2. NADP catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-1873-MONOMER.
SABIO-RKO28440.
UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable L-aspartate dehydrogenase (EC:1.4.1.21)
Gene namesi
Name:nadX
Ordered Locus Names:AF_1838
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Probable L-aspartate dehydrogenaseUniRule annotationPRO_0000144894Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224325.AF1838.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi10 – 2112
Beta strandi25 – 306
Beta strandi39 – 424
Helixi43 – 464
Beta strandi52 – 565
Helixi60 – 7213
Beta strandi76 – 805
Helixi82 – 865
Helixi88 – 10114
Beta strandi105 – 1073
Helixi115 – 1206
Helixi122 – 1243
Beta strandi125 – 13511
Helixi136 – 1383
Beta strandi143 – 1497
Helixi150 – 1567
Helixi162 – 17110
Beta strandi176 – 1838
Beta strandi185 – 19511
Beta strandi198 – 2069
Beta strandi212 – 2165
Helixi217 – 23115
Beta strandi232 – 2354

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DC1X-ray1.90A/B1-236[»]
ProteinModelPortaliO28440.
SMRiO28440. Positions 1-236.

Miscellaneous databases

EvolutionaryTraceiO28440.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1712.
KOiK06989.
OMAiECAGHSA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01265. NadX.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsiTIGR03855. NAD_NadX. 1 hit.

Sequencei

Sequence statusi: Complete.

O28440-1 [UniParc]FASTAAdd to Basket

« Hide

MLVGLIGYGA IGKFLAEWLE RNGFEIAAIL DVRGEHEKMV RGIDEFLQRE    50
MDVAVEAASQ QAVKDYAEKI LKAGIDLIVL STGAFADRDF LSRVREVCRK 100
TGRRVYIASG AIGGLDAIFS ASELIEEIVL TTRKNWRQFG RKGVIFEGSA 150
SEAAQKFPKN LNVAATLSIA SGKDVKVRLV ADEVEENIHE ILVRGEFGEM 200
EIRVRNRPMR ENPKTSYLAA LSVTRILRNL KEGLVV 236
Length:236
Mass (Da):26,208
Last modified:January 1, 1998 - v1
Checksum:i29218ACC7F919F52
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000782 Genomic DNA. Translation: AAB89415.1.
PIRiE69479.
RefSeqiNP_070664.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89415; AAB89415; AF_1838.
GeneIDi1485059.
KEGGiafu:AF1838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000782 Genomic DNA. Translation: AAB89415.1 .
PIRi E69479.
RefSeqi NP_070664.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DC1 X-ray 1.90 A/B 1-236 [» ]
ProteinModelPortali O28440.
SMRi O28440. Positions 1-236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224325.AF1838.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB89415 ; AAB89415 ; AF_1838 .
GeneIDi 1485059.
KEGGi afu:AF1838.

Phylogenomic databases

eggNOGi COG1712.
KOi K06989.
OMAi ECAGHSA.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci AFUL224325:GJBC-1873-MONOMER.
SABIO-RK O28440.

Miscellaneous databases

EvolutionaryTracei O28440.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_01265. NadX.
InterProi IPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsi TIGR03855. NAD_NadX. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Entry informationi

Entry nameiASPD_ARCFU
AccessioniPrimary (citable) accession number: O28440
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3